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P08514 (ITA2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 188. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Integrin alpha-IIb
Alternative name(s):
GPalpha IIb
Short name=GPIIb
Platelet membrane glycoprotein IIb
CD_antigen=CD41
Gene names
Name:ITGA2B
Synonyms:GP2B, ITGAB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1039 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. It recognizes the sequence R-G-D in a wide array of ligands. It recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial cell surface.

Subunit structure

Heterodimer of an alpha and a beta subunit. The alpha subunit is composed of a heavy and a light chain linked by a disulfide bond. Alpha-IIb associates with beta-3. Directly interacts with RNF181. Interacts (via C-terminus cytoplasmic tail region) with CIB1; the interaction is direct and calcium-dependent. Interacts (via C-terminus cytoplasmic tail region) with CIB2, CIB3 and CIB4; the interactions are stabilized/increased in a calcium and magnesium-dependent manner. Ref.20 Ref.21 Ref.24 Ref.25 Ref.26 Ref.27

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Isoform 1 and isoform 2 were identified in platelets and megakaryocytes, but not in reticulocytes or in Jurkat and U-937 white blood cell line. Isoform 3 is expressed by leukemia, prostate adenocarcinoma and melanoma cells but not by platelets or normal prostate or breast epithelial cells.

Polymorphism

Position 874 is associated with platelet-specific alloantigen HPA-3/BAK/LEK. HPA-3A/BAK(A)/LEK(A) has Ile-874 and HPA-3B/BAK(B)/LEK(B) has Ser-874. HPA-3B is involved in neonatal alloimmune thrombocytopenia (NAIT or NATP).

Involvement in disease

Glanzmann thrombasthenia (GT) [MIM:273800]: A common inherited disease of platelet aggregation. It is characterized by mucocutaneous bleeding of mild-to-moderate severity. GT has been classified clinically into types I and II. In type I, platelets show absence of the glycoprotein IIb-IIIa complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express the GPIIb-IIIa complex at reduced levels, have detectable amounts of fibrinogen, and have low or moderate clot retraction capability.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.38 Ref.39 Ref.41 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.48 Ref.49 Ref.50 Ref.51 Ref.52

Bleeding disorder, platelet-type 16 (BDPLT16) [MIM:187800]: An autosomal dominant form of congenital macrothrombocytopenia associated with platelet anisocytosis. It is a disorder of platelet production. Affected individuals may have no or only mildly increased bleeding tendency. In vitro studies show mild platelet functional abnormalities.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.37 Ref.53

Sequence similarities

Belongs to the integrin alpha chain family.

Contains 7 FG-GAP repeats.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   Molecular functionIntegrin
Receptor
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Pyrrolidone carboxylic acid
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

cell adhesion

Traceable author statement PubMed 10429193Ref.1. Source: ProtInc

cell-matrix adhesion

Inferred from electronic annotation. Source: Ensembl

extracellular matrix organization

Traceable author statement. Source: Reactome

integrin-mediated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

platelet activation

Traceable author statement. Source: Reactome

platelet aggregation

Inferred from electronic annotation. Source: Ensembl

platelet degranulation

Traceable author statement. Source: Reactome

positive regulation of leukocyte migration

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

focal adhesion

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

integrin complex

Inferred from electronic annotation. Source: InterPro

plasma membrane

Traceable author statement. Source: Reactome

platelet alpha granule membrane

Traceable author statement. Source: Reactome

   Molecular_functionextracellular matrix binding

Inferred from electronic annotation. Source: Ensembl

identical protein binding

Inferred from physical interaction PubMed 11606749PubMed 14681217PubMed 15067009. Source: IntAct

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 14681217PubMed 15379538PubMed 19279667. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself7EBI-702693,EBI-702693
ITGB3P0510611EBI-702693,EBI-702847

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P08514-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P08514-2)

The sequence of this isoform differs from the canonical sequence as follows:
     948-981: Missing.
Isoform 3 (identifier: P08514-3)

The sequence of this isoform differs from the canonical sequence as follows:
     910-1039: SCDSAPCTVV...PLEEDDEEGE → VSRLSGLWPG...ATLGPWEHFK

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Ref.11 Ref.12
Chain32 – 10391008Integrin alpha-IIb
PRO_0000016275
Chain32 – 887856Integrin alpha-IIb heavy chain
PRO_0000016276
Chain891 – 1039149Integrin alpha-IIb light chain, form 1
PRO_0000292348
Chain903 – 1039137Integrin alpha-IIb light chain, form 2
PRO_0000016277

Regions

Topological domain32 – 993962Extracellular Potential
Transmembrane994 – 101926Helical; Potential
Topological domain1020 – 103920Cytoplasmic Potential
Repeat35 – 9662FG-GAP 1
Repeat110 – 17364FG-GAP 2
Repeat186 – 23853FG-GAP 3
Repeat251 – 31060FG-GAP 4
Repeat311 – 37161FG-GAP 5
Repeat373 – 43260FG-GAP 6
Repeat434 – 49663FG-GAP 7
Calcium binding274 – 2829 Potential
Calcium binding328 – 3369 Potential
Calcium binding396 – 4049 Potential
Calcium binding457 – 4659 Potential
Motif1022 – 10265GFFKR motif

Amino acid modifications

Modified residue8911Pyrrolidone carboxylic acid; in light chain form 1
Glycosylation461N-linked (GlcNAc...) Ref.16
Glycosylation2801N-linked (GlcNAc...) Ref.16
Glycosylation6011N-linked (GlcNAc...) Ref.16 Ref.23
Glycosylation7111N-linked (GlcNAc...) Ref.16
Glycosylation8741O-linked (GalNAc...); in alloantigen HPA-3B
Glycosylation8781O-linked (GalNAc...) Ref.17
Glycosylation9621N-linked (GlcNAc...)
Disulfide bond87 ↔ 96 Ref.16
Disulfide bond138 ↔ 161 Ref.16
Disulfide bond177 ↔ 198 Ref.16
Disulfide bond504 ↔ 515 Ref.16
Disulfide bond521 ↔ 576 Ref.16
Disulfide bond633 ↔ 639 Ref.16
Disulfide bond705 ↔ 718 Ref.16
Disulfide bond857 ↔ 911Interchain (between heavy and light chains) Ref.16
Disulfide bond916 ↔ 921 Ref.16

Natural variations

Alternative sequence910 – 1039130SCDSA…DEEGE → VSRLSGLWPGLPGTHGAEGM GGGRGVRVCCGPLWATLGPW EHFK in isoform 3.
VSP_002736
Alternative sequence948 – 98134Missing in isoform 2.
VSP_002737
Natural variant401T → I. Ref.40
Corresponds to variant rs5915 [ dbSNP | Ensembl ].
VAR_014176
Natural variant861L → P in GT; cells co-transfected with mutated alpha-IIb and wild-type beta-3 scarcely expressed the alpha-IIb/beta-3 complex. Ref.45
VAR_030445
Natural variant1391A → V in GT. Ref.46
VAR_030446
Natural variant1611C → W in GT. Ref.44
VAR_030447
Natural variant1741Y → H in GT; abolishes the binding function of alpha-IIb/beta-3 for soluble ligands without disturbing alpha-IIb/beta-3 expression; functional defect is likely caused by its allosteric effect rather than by a defect in the ligand-binding site itself. Ref.48
VAR_030448
Natural variant1761P → A in GT; impairs surface expression of alpha-IIb/beta-3 and abrogates ligand binding to the activated integrin. Ref.43 Ref.46
VAR_009885
Natural variant1761P → L in GT; impairs surface expression of alpha-IIb/beta-3. Ref.43
VAR_009886
Natural variant2021F → C in GT; associated with abrogation of alpha-IIb/beta-3 complex formation. Ref.50
VAR_030449
Natural variant2071T → I in GT. Ref.34
VAR_030450
Natural variant2141L → P in GT; disrupts the structural conformation and the ligand binding properties of the heterodimeric complex; in addition the mutation appears to confer susceptibility to proteolysis. Ref.35
VAR_030451
Natural variant2221F → L in GT. Ref.44
VAR_030452
Natural variant2671G → E in GT. Ref.46
VAR_030453
Natural variant2731G → D in GT; alters the heterodimer conformation thus impairing their intracellular transport. Ref.30
VAR_003979
Natural variant3131G → A. Ref.1 Ref.2
Corresponds to variant rs1126554 [ dbSNP | Ensembl ].
VAR_054820
Natural variant3201F → S in GT; type I; impairs surface expression of alpha-IIb/beta-3. Ref.38
VAR_009887
Natural variant3291V → F in GT; expression of mutant subunit alpha-IIb/bet-3 is 28% of control; mutant pro-alpha-IIb subunit is retained in the endoplasmic reticulum. Ref.47
VAR_030454
Natural variant3551E → K in GT; type I; impairs surface expression of alpha-IIb/beta-3. Ref.38 Ref.39
VAR_009888
Natural variant3581R → H in GT; type II. Ref.32
VAR_003980
Natural variant3801G → D in GT. Ref.46
VAR_030455
Natural variant4051I → T in GT; expression of mutant subunit alpha-IIb/bet-3 is 11% of control; mutant pro-alpha-IIb subunit is retained in the endoplasmic reticulum. Ref.46 Ref.47 Ref.52
VAR_030456
Natural variant4121G → R in GT. Ref.44
VAR_030457
Natural variant4491G → D in GT; type I. Ref.31
VAR_003981
Natural variant456 – 4572Missing in GT; alteres the conformation of heterodimers such that they were neither recognized by the heterodimer-specific antibody A2A9 nor able to undergo further intracellular processing or transport to the cell surface.
VAR_030458
Natural variant5811A → D in GT. Ref.46
VAR_030459
Natural variant5961I → T in GT; type I. Ref.34 Ref.39 Ref.52
VAR_030460
Natural variant6491V → L.
Corresponds to variant rs7207402 [ dbSNP | Ensembl ].
VAR_054821
Natural variant7051C → R in GT; type II; the rate of subunit maturation and the surface exposure of ghlycoprotein IIb/beta-3 are strongly reduced. Ref.41 Ref.46 Ref.52
VAR_030461
Natural variant7521L → V in GT. Ref.46
VAR_030462
Natural variant7551R → P in GT. Ref.46
VAR_030463
Natural variant7781Q → P in GT; type II. Ref.36 Ref.38 Ref.52
VAR_003982
Natural variant8471L → P in GT. Ref.44
VAR_030464
Natural variant8741I → S Alloantigen HPA-3B. Ref.40
Corresponds to variant rs5911 [ dbSNP | Ensembl ].
VAR_003983
Natural variant9341V → F in GT; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface consistent with a severe type 1 phenotype. Ref.52
VAR_069917
Natural variant9431P → L in GT; marked reduction in the rate of surface expression. Ref.51
VAR_030465
Natural variant9571S → L in GT; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface consistent with a severe type 1 phenotype; the mutation may interfere with correct folding of the protein. Ref.52
VAR_069918
Natural variant9681Y → N. Ref.40
Corresponds to variant rs5914 [ dbSNP | Ensembl ].
VAR_014177
Natural variant9821V → M in GT; much reduced surface expression of alpha-IIb/beta-3 and a block in the maturation of pro-alpha-IIb. Ref.49 Ref.52
VAR_030466
Natural variant9891A → T. Ref.49 Ref.52
Corresponds to variant rs78165611 [ dbSNP | Ensembl ].
VAR_030467
Natural variant10261R → Q in GT and BDPLT16; results in low surface expression of the mutant protein. Ref.34 Ref.37
VAR_030468
Natural variant10261R → W in BDPLT16; results in abnormal membrane ruffling and cytoplasmic protrusions as well as defective proplatelet formation. Ref.53
VAR_069919

Experimental info

Mutagenesis1029 – 10302PP → AA: Imparts constitutive activity (ligand-binding) to alpha-IIb/beta-3. Ref.22
Sequence conflict231P → A in AAA35926. Ref.2
Sequence conflict1201A → S in BAG37735. Ref.4
Sequence conflict287 – 2882GA → VP in AAA53150. Ref.3
Sequence conflict3461E → D in AAA35926. Ref.2
Sequence conflict5651N → D in AAA35926. Ref.2
Sequence conflict5661L → V in CAA29987. Ref.8
Sequence conflict6331C → S in AAA60114. Ref.1
Sequence conflict7291Q → E in CAA29987. Ref.8
Sequence conflict9711P → A in AAA53150. Ref.3
Sequence conflict10291P → H in AAA35926. Ref.2
Sequence conflict10291P → H in AAA52588. Ref.10
Sequence conflict10301P → T in AAA52588. Ref.10

Secondary structure

.............................................................................................................................................................................................. 1039
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 14, 2009. Version 3.
Checksum: 063EE298E026F116

FASTA1,039113,377
        10         20         30         40         50         60 
MARALCPLQA LWLLEWVLLL LGPCAAPPAW ALNLDPVQLT FYAGPNGSQF GFSLDFHKDS 

        70         80         90        100        110        120 
HGRVAIVVGA PRTLGPSQEE TGGVFLCPWR AEGGQCPSLL FDLRDETRNV GSQTLQTFKA 

       130        140        150        160        170        180 
RQGLGASVVS WSDVIVACAP WQHWNVLEKT EEAEKTPVGS CFLAQPESGR RAEYSPCRGN 

       190        200        210        220        230        240 
TLSRIYVEND FSWDKRYCEA GFSSVVTQAG ELVLGAPGGY YFLGLLAQAP VADIFSSYRP 

       250        260        270        280        290        300 
GILLWHVSSQ SLSFDSSNPE YFDGYWGYSV AVGEFDGDLN TTEYVVGAPT WSWTLGAVEI 

       310        320        330        340        350        360 
LDSYYQRLHR LRGEQMASYF GHSVAVTDVN GDGRHDLLVG APLYMESRAD RKLAEVGRVY 

       370        380        390        400        410        420 
LFLQPRGPHA LGAPSLLLTG TQLYGRFGSA IAPLGDLDRD GYNDIAVAAP YGGPSGRGQV 

       430        440        450        460        470        480 
LVFLGQSEGL RSRPSQVLDS PFPTGSAFGF SLRGAVDIDD NGYPDLIVGA YGANQVAVYR 

       490        500        510        520        530        540 
AQPVVKASVQ LLVQDSLNPA VKSCVLPQTK TPVSCFNIQM CVGATGHNIP QKLSLNAELQ 

       550        560        570        580        590        600 
LDRQKPRQGR RVLLLGSQQA GTTLNLDLGG KHSPICHTTM AFLRDEADFR DKLSPIVLSL 

       610        620        630        640        650        660 
NVSLPPTEAG MAPAVVLHGD THVQEQTRIV LDCGEDDVCV PQLQLTASVT GSPLLVGADN 

       670        680        690        700        710        720 
VLELQMDAAN EGEGAYEAEL AVHLPQGAHY MRALSNVEGF ERLICNQKKE NETRVVLCEL 

       730        740        750        760        770        780 
GNPMKKNAQI GIAMLVSVGN LEEAGESVSF QLQIRSKNSQ NPNSKIVLLD VPVRAEAQVE 

       790        800        810        820        830        840 
LRGNSFPASL VVAAEEGERE QNSLDSWGPK VEHTYELHNN GPGTVNGLHL SIHLPGQSQP 

       850        860        870        880        890        900 
SDLLYILDIQ PQGGLQCFPQ PPVNPLKVDW GLPIPSPSPI HPAHHKRDRR QIFLPEPEQP 

       910        920        930        940        950        960 
SRLQDPVLVS CDSAPCTVVQ CDLQEMARGQ RAMVTVLAFL WLPSLYQRPL DQFVLQSHAW 

       970        980        990       1000       1010       1020 
FNVSSLPYAV PPLSLPRGEA QVWTQLLRAL EERAIPIWWV LVGVLGGLLL LTILVLAMWK 

      1030 
VGFFKRNRPP LEEDDEEGE 

« Hide

Isoform 2 [UniParc].

Checksum: 81C09F0D904CB534
Show »

FASTA1,005109,574
Isoform 3 [UniParc].

Checksum: 0100D4C5919320BE
Show »

FASTA953103,218

References

« Hide 'large scale' references
[1]"Structure of the platelet membrane glycoprotein IIb. Homology to the alpha subunits of the vitronectin and fibronectin membrane receptors."
Poncz M., Eisman R., Heidenreich R., Silver S.M., Vilaire G., Surrey S., Schwartz E., Bennett J.S.
J. Biol. Chem. 262:8476-8482(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-313.
[2]"GPIIb and GPIIIa amino acid sequences deduced from human megakaryocyte cDNAs."
Frachet P., Uzan G., Thevenon D., Denarier E., Prandini M.H., Marguerie G.
Mol. Biol. Rep. 14:27-33(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-313.
[3]"Organization of the gene for platelet glycoprotein IIb."
Heidenreich R., Eisman R., Surrey S., Delgrosso K., Bennett J.S., Schwartz E., Poncz M.
Biochemistry 29:1232-1244(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Spleen.
[5]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Lung.
[7]"Human platelets and megakaryocytes contain alternately spliced glycoprotein IIb mRNAs."
Bray P.F., Leung C.S.-I., Shuman M.A.
J. Biol. Chem. 265:9587-9590(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
Tissue: Erythroleukemia.
[8]"cDNA clones for human platelet GPIIb corresponding to mRNA from megakaryocytes and HEL cells. Evidence for an extensive homology to other Arg-Gly-Asp adhesion receptors."
Uzan G., Frachet P., Lajmanovich A., Prandini M.-H., Denarier E., Duperray A., Loftus J., Ginsberg M., Plow E., Marguerie G.
Eur. J. Biochem. 171:87-93(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 392-1039 (ISOFORM 1).
[9]"Platelet glycoprotein IIb. Chromosomal localization and tissue expression."
Bray P.F., Rosa J.P., Johnston G.I., Shiu D.T., Cook R.G., Lau C., Kan Y.W., McEver R.P., Shuman M.A.
J. Clin. Invest. 80:1812-1817(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 868-1039 (ISOFORM 1).
[10]"Isolation of the human platelet glycoprotein IIb gene and characterization of the 5' flanking region."
Prandini M.H., Denarier E., Frachet P., Uzan G., Marguerie G.
Biochem. Biophys. Res. Commun. 156:595-601(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-62 AND 1021-1039.
[11]"Platelet glycoproteins IIb and IIIa: evidence for a family of immunologically and structurally related glycoproteins in mammalian cells."
Charo I.F., Fitzgerald L.A., Steiner B., Rall S.C., Bekeart L.S., Phillips D.R.
Proc. Natl. Acad. Sci. U.S.A. 83:8351-8355(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 32-56 AND 903-917.
[12]"Separation of important new platelet glycoproteins (GPIa, GPIc, GPIc*, GPIIa and GMP-140) by F.P.L.C. Characterization by monoclonal antibodies and gas-phase sequencing."
Catimel B., Parmentier S., Leung L.L., McGregor J.L.
Biochem. J. 279:419-425(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 32-42.
[13]"Thermal stability of individual domains in platelet glycoprotein IIbIIIa."
Makogonenko E.M., Yakubenko V.P., Ingham K.C., Medved L.V.
Eur. J. Biochem. 237:205-211(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 32 AND 872.
[14]"Purification and partial amino acid sequence of human platelet membrane glycoproteins IIb and IIIa."
Hiraiwa A., Matsukage A., Shiku H., Takahashi T., Naito K., Yamada K.
Blood 69:560-564(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 487-501 AND 1026-1038.
[15]"Interchain and intrachain disulphide bonds in human platelet glycoprotein IIb. Localization of the epitopes for several monoclonal antibodies."
Calvete J.J., Alvarez M.V., Rivas G., Hew C.L., Henschen A., Gonzalez-Rodriguez J.
Biochem. J. 261:551-560(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 903-922 AND 934-939.
[16]"Complete localization of the intrachain disulphide bonds and the N-glycosylation points in the alpha-subunit of human platelet glycoprotein IIb."
Calvete J.J., Henschen A., Gonzalez-Rodriguez J.
Biochem. J. 261:561-568(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-46; ASN-280; ASN-601 AND ASN-711.
[17]"Localization of an O-glycosylation site in the alpha-subunit of the human platelet integrin GPIIb/IIIa involved in Baka (HPA-3a) alloantigen expression."
Calvete J.J., Muniz-Diaz E.
FEBS Lett. 328:30-34(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT SER-878.
[18]"Identification of a novel truncated alphaIIb integrin."
Trikha M., Cai Y., Grignon D., Honn K.V.
Cancer Res. 58:4771-4775(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[19]"Characterization of the beta-chain N-terminus heterogeneity and the alpha-chain C-terminus of human platelet GPIIb. Posttranslational cleavage sites."
Calvete J.J., Schafer W., Henschen A., Gonzalez-Rodriguez J.
FEBS Lett. 272:37-40(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC CLEAVAGE, PYROGLUTAMATE FORMATION AT GLN-891.
[20]"Identification of a novel calcium-binding protein that interacts with the integrin alphaIIb cytoplasmic domain."
Naik U.P., Patel P.M., Parise L.V.
J. Biol. Chem. 272:4651-4654(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CIB1.
Tissue: Fetal liver.
[21]"Calcium-dependent properties of CIB binding to the integrin alphaIIb cytoplasmic domain and translocation to the platelet cytoskeleton."
Shock D.D., Naik U.P., Brittain J.E., Alahari S.K., Sondek J., Parise L.V.
Biochem. J. 342:729-735(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CIB1.
[22]"Bidirectional transmembrane modulation of integrin alphaIIbbeta3 conformations."
Leisner T.M., Wencel-Drake J.D., Wang W., Lam S.C.
J. Biol. Chem. 274:12945-12949(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF 1029-PRO-PRO-1030.
[23]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-601.
Tissue: Plasma.
[24]"RN181, a novel ubiquitin E3 ligase that interacts with the KVGFFKR motif of platelet integrin alpha(IIb)beta3."
Brophy T.M., Raab M., Daxecker H., Culligan K.G., Lehmann I., Chubb A.J., Treumann A., Moran N.
Biochem. Biophys. Res. Commun. 369:1088-1093(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNF181.
[25]"Solution structures of Ca2+-CIB1 and Mg2+-CIB1 and their interactions with the platelet integrin alphaIIb cytoplasmic domain."
Huang H., Ishida H., Yamniuk A.P., Vogel H.J.
J. Biol. Chem. 286:17181-17192(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CIB1.
[26]"Biophysical and structural studies of the human calcium- and integrin-binding protein family: understanding their functional similarities and differences."
Huang H., Bogstie J.N., Vogel H.J.
Biochem. Cell Biol. 90:646-656(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CIB1; CIB2; CIB3 AND CIB4.
[27]"Structural basis for the activation of platelet integrin alphaIIbbeta3 by calcium- and integrin-binding protein 1."
Huang H., Vogel H.J.
J. Am. Chem. Soc. 134:3864-3872(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CIB1.
[28]"Inherited diseases of platelet glycoproteins: considerations for rapid molecular characterization."
Bray P.F.
Thromb. Haemost. 72:492-502(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON GT VARIANTS.
[29]"Polymorphism of human platelet membrane glycoprotein IIb associated with the Baka/Bakb alloantigen system."
Lyman S., Aster R.H., Visentin G.P., Newman P.J.
Blood 75:2343-2348(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HPA-3 (BAK).
[30]"Glanzmann thrombasthenia secondary to a Gly273-->Asp mutation adjacent to the first calcium-binding domain of platelet glycoprotein IIb."
Poncz M., Rifat S., Coller B.S., Newman P.J., Shattil S.J., Parrella T., Fortina P., Bennett J.S.
J. Clin. Invest. 93:172-179(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GT ASP-273.
[31]"A single amino acid substitution flanking the fourth calcium binding domain of alpha IIb prevents maturation of the alpha IIb beta 3 integrin complex."
Wilcox D.A., Wautier J.-L., Pidard D., Newman P.J.
J. Biol. Chem. 269:4450-4457(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GT ASP-449.
[32]"Glanzmann thrombasthenia resulting from a single amino acid substitution between the second and third calcium-binding domains of GPIIb. Role of the GPIIb amino terminus in integrin subunit association."
Wilcox D.A., Paddock C.M., Lyman S., Gill J.C., Newman P.J.
J. Clin. Invest. 95:1553-1560(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GT HIS-358.
[33]"Glanzmann thrombasthenia due to a two amino acid deletion in the fourth calcium-binding domain of alpha IIb: demonstration of the importance of calcium-binding domains in the conformation of alpha IIb beta 3."
Basani R.B., Vilaire G., Shattil S.J., Kolodziej M.A., Bennett J.S., Poncz M.
Blood 88:167-173(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GT VAL-456-457-ASP DEL, CHARACTERIZATION OF VARIANT GT VAL-456-457-ASP DEL.
[34]"Hematologically important mutations: Glanzmann thrombasthenia."
French D.L., Coller B.S.
Blood Cells Mol. Dis. 23:39-51(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GT ILE-207; THR-596 AND GLN-1026.
[35]"Glycoprotein IIb Leu214Pro mutation produces Glanzmann thrombasthenia with both quantitative and qualitative abnormalities in GPIIb/IIIa."
Grimaldi C.M., Chen F., Wu C., Weiss H.J., Coller B.S., French D.L.
Blood 91:1562-1571(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GT PRO-214, CHARACTERIZATION OF VARIANT GT PRO-214.
[36]"A Gln747-->Pro substitution in the IIb subunit is responsible for a moderate IIbbeta3 deficiency in Glanzmann thrombasthenia."
Tadokoro S., Tomiyama Y., Honda S., Arai M., Yamamoto N., Shiraga M., Kosugi S., Kanakura Y., Kurata Y., Matsuzawa Y.
Blood 92:2750-2758(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GT PRO-778.
[37]"R to Q amino acid substitution in the GFFKR sequence of the cytoplasmic domain of the integrin IIb subunit in a patient with a Glanzmann's thrombasthenia-like syndrome."
Peyruchaud O., Nurden A.T., Milet S., Macchi L., Pannochia A., Bray P.F., Kieffer N., Bourre F.
Blood 92:4178-4187(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BDPLT16 GLN-1026, CHARACTERIZATION OF VARIANT BDPLT16 GLN-1026.
[38]"Novel point mutations in the alphaIIb subunit (Phe289-->Ser, Glu324-->Lys and Gln747-->Pro) causing thrombasthenic phenotypes in four Japanese patients."
Ambo H., Kamata T., Handa M., Kawai Y., Oda A., Murata M., Takada Y., Ikeda Y.
Br. J. Haematol. 102:829-840(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GT SER-320; LYS-355 AND PRO-778.
[39]"Double heterozygosity of the GPIIb gene in a Swiss patient with Glanzmann's thrombasthenia."
Ruan J., Peyruchaud O., Alberio L., Valles G., Clemetson K., Bourre F., Nurden A.T.
Br. J. Haematol. 102:918-925(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GT LYS-355 AND THR-596.
[40]"Characterization of single-nucleotide polymorphisms in coding regions of human genes."
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ILE-40; SER-874 AND ASN-968.
[41]"Molecular genetic analysis of a compound heterozygote for the glycoprotein (GP) IIb gene associated with Glanzmann's thrombasthenia: disruption of the 674-687 disulfide bridge in GPIIb prevents surface exposure of GPIIb-IIIa complexes."
Gonzalez-Manchon C., Fernandez-Pinel M., Arias-Salgado E.G., Ferrer M., Alvarez M.-V., Garcia-Munoz S., Ayuso M.S., Parrilla R.
Blood 93:866-875(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GT ARG-705, CHARACTERIZATION OF VARIANT GT ARG-705.
[42]Erratum
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 23:373-373(1999)
[43]"A naturally occurring mutation near the amino terminus of alphaIIb defines a new region involved in ligand binding to alphaIIbbeta3."
Basani R.B., French D.L., Vilaire G., Brown D.L., Chen F., Coller B.S., Derrick J.M., Gartner T.K., Bennett J.S., Poncz M.
Blood 95:180-188(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GT ALA-176 AND LEU-176.
[44]"Description of 10 new mutations in platelet glycoprotein IIb (alphaIIb) and glycoprotein IIIa (beta3) genes."
Vinciguerra C., Bordet J.C., Beaune G., Grenier C., Dechavanne M., Negrier C.
Platelets 12:486-495(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GT TRP-161; LEU-222; ARG-412 AND PRO-847.
[45]"A Leu55 to Pro substitution in the integrin alphaIIb is responsible for a case of Glanzmann's thrombasthenia."
Tanaka S., Hayashi T., Hori Y., Terada C., Han K.S., Ahn H.S., Bourre F., Tani Y.
Br. J. Haematol. 118:833-835(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GT PRO-86, CHARACTERIZATION OF VARIANT GT PRO-86.
[46]"Glanzmann's thrombasthenia: identification of 19 new mutations in 30 patients."
D'Andrea G., Colaizzo D., Vecchione G., Grandone E., Di Minno G., Margaglione M.
Thromb. Haemost. 87:1034-1042(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GT VAL-139; ALA-176; GLU-267; ASP-380; THR-405; ASP-581; ARG-705; VAL-752 AND PRO-755.
[47]"Two novel mutations in the alpha IIb calcium-binding domains identify hydrophobic regions essential for alpha IIbbeta 3 biogenesis."
Mitchell W.B., Li J.H., Singh F., Michelson A.D., Bussel J., Coller B.S., French D.L.
Blood 101:2268-2276(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GT PHE-329 AND THR-405, CHARACTERIZATION OF VARIANTS GT PHE-329 AND THR-405.
[48]"A naturally occurring Tyr143His alpha IIb mutation abolishes alpha IIb beta 3 function for soluble ligands but retains its ability for mediating cell adhesion and clot retraction: comparison with other mutations causing ligand-binding defects."
Kiyoi T., Tomiyama Y., Honda S., Tadokoro S., Arai M., Kashiwagi H., Kosugi S., Kato H., Kurata Y., Matsuzawa Y.
Blood 101:3485-3491(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GT HIS-174, CHARACTERIZATION OF VARIANT GT HIS-174.
[49]"Triple heterozygosity in the integrin alphaIIb subunit in a patient with Glanzmann's thrombasthenia."
Nurden A.T., Breillat C., Jacquelin B., Combrie R., Freedman J., Blanchette V.S., Schmugge M., Rand M.L.
J. Thromb. Haemost. 2:813-819(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GT MET-982, CHARACTERIZATION OF VARIANT GT MET-982, VARIANT THR-989.
[50]"A novel Phe171Cys mutation in integrin alpha causes Glanzmann thrombasthenia by abrogating alphaIIbbeta3 complex formation."
Rosenberg N., Landau M., Luboshitz J., Rechavi G., Seligsohn U.
J. Thromb. Haemost. 2:1167-1175(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GT CYS-202, CHARACTERIZATION OF VARIANT GT CYS-202.
[51]"Type II Glanzmann thrombasthenia in a compound heterozygote for the alpha IIb gene. A novel missense mutation in exon 27."
Jayo A., Pabon D., Lastres P., Jimenez-Yuste V., Gonzalez-Manchon C.
Haematologica 91:1352-1359(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GT LEU-943, CHARACTERIZATION OF VARIANT GT LEU-943.
[52]"AlphaIIbbeta3 integrin: new allelic variants in Glanzmann thrombasthenia, effects on ITGA2B and ITGB3 mRNA splicing, expression, and structure-function."
Jallu V., Dusseaux M., Panzer S., Torchet M.F., Hezard N., Goudemand J., de Brevern A.G., Kaplan C.
Hum. Mutat. 31:237-246(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GT THR-405; THR-596; ARG-705; PRO-778; PHE-934; LEU-957; MET-982 AND THR-989, CHARACTERIZATION OF VARIANTS GT PHE-934 AND LEU-957.
[53]"Heterozygous ITGA2B R995W mutation inducing constitutive activation of the alphaIIbbeta3 receptor affects proplatelet formation and causes congenital macrothrombocytopenia."
Kunishima S., Kashiwagi H., Otsu M., Takayama N., Eto K., Onodera M., Miyajima Y., Takamatsu Y., Suzumiya J., Matsubara K., Tomiyama Y., Saito H.
Blood 117:5479-5484(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BDPLT16 TRP-1026, CHARACTERIZATION OF VARIANT BDPLT16 TRP-1026.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02764 mRNA. Translation: AAA60114.1.
M34480 mRNA. Translation: AAA35926.1.
M34344, M33319, M33320 Genomic DNA. Translation: AAA53150.1.
M54799 Genomic DNA. Translation: AAA52599.1.
X06831 mRNA. Translation: CAA29987.1.
M18085 mRNA. Translation: AAA52597.1.
M22568 Genomic DNA. Translation: AAA52587.1.
M22569 Genomic DNA. Translation: AAA52588.1.
AF098114 mRNA. Translation: AAC98507.1.
AK315335 mRNA. Translation: BAG37735.1.
AC003043 Genomic DNA. No translation available.
BC117443 mRNA. Translation: AAI17444.1.
BC126442 mRNA. Translation: AAI26443.1.
CCDSCCDS32665.1. [P08514-1]
PIRA34269.
RefSeqNP_000410.2. NM_000419.3. [P08514-1]
UniGeneHs.411312.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DPKNMR-A1020-1039[»]
1DPQNMR-A1020-1039[»]
1JX5model-A32-483[»]
1KUPNMR-A1018-1028[»]
1KUZNMR-A1018-1028[»]
1M8ONMR-A1020-1039[»]
1RN0model-A32-482[»]
1S4WNMR-A1020-1039[»]
1TYEX-ray2.90A/C/E32-483[»]
1UV9model-A32-973[»]
2K1ANMR-A989-1029[»]
2K9JNMR-A989-1029[»]
2KNCNMR-A991-1039[»]
2VC2X-ray3.10A32-483[»]
2VDKX-ray2.80A32-483[»]
2VDLX-ray2.75A32-483[»]
2VDMX-ray2.90A32-483[»]
2VDNX-ray2.90A32-483[»]
2VDOX-ray2.51A32-483[»]
2VDPX-ray2.80A32-483[»]
2VDQX-ray2.59A32-483[»]
2VDRX-ray2.40A32-483[»]
3FCSX-ray2.55A/C32-989[»]
3FCUX-ray2.90A/C/E32-488[»]
3NIDX-ray2.30A/C32-488[»]
3NIFX-ray2.40A/C32-488[»]
3NIGX-ray2.25A/C32-488[»]
3T3MX-ray2.60A/C32-488[»]
3T3PX-ray2.20A/C32-488[»]
3ZDXX-ray2.45A/C32-488[»]
3ZDYX-ray2.45A/C32-488[»]
3ZDZX-ray2.75A/C32-488[»]
3ZE0X-ray2.95A/C32-488[»]
3ZE1X-ray3.00A/C32-488[»]
3ZE2X-ray2.35A/C32-488[»]
4CAKelectron microscopy20.50A32-989[»]
ProteinModelPortalP08514.
SMRP08514. Positions 32-989, 991-1039.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109881. 10 interactions.
DIPDIP-68N.
IntActP08514. 1 interaction.
STRING9606.ENSP00000262407.

Chemistry

BindingDBP08514.
ChEMBLCHEMBL2111443.
DrugBankDB00775. Tirofiban.

PTM databases

PhosphoSiteP08514.

Polymorphism databases

DMDM226694183.

2D gel databases

OGPP08514.

Proteomic databases

PaxDbP08514.
PRIDEP08514.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262407; ENSP00000262407; ENSG00000005961. [P08514-1]
ENST00000353281; ENSP00000340536; ENSG00000005961. [P08514-2]
GeneID3674.
KEGGhsa:3674.
UCSCuc002igt.1. human. [P08514-1]

Organism-specific databases

CTD3674.
GeneCardsGC17M042460.
HGNCHGNC:6138. ITGA2B.
HPACAB018611.
HPA031168.
HPA031169.
HPA031170.
HPA031171.
MIM187800. phenotype.
273800. phenotype.
607759. gene.
neXtProtNX_P08514.
Orphanet140957. Autosomal dominant macrothrombocytopenia.
853. Fetal and neonatal alloimmune thrombocytopenia.
849. Glanzmann thrombasthenia.
PharmGKBPA29938.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG26407.
HOGENOMHOG000231603.
HOVERGENHBG006186.
InParanoidP08514.
KOK06476.
OMACFNIQMC.
OrthoDBEOG7TMZQZ.
PhylomeDBP08514.
TreeFamTF105391.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.
REACT_604. Hemostasis.
SignaLinkP08514.

Gene expression databases

ArrayExpressP08514.
BgeeP08514.
CleanExHS_ITGA2B.
GenevestigatorP08514.

Family and domain databases

InterProIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
[Graphical view]
PfamPF01839. FG-GAP. 1 hit.
PF00357. Integrin_alpha. 1 hit.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]
PRINTSPR01185. INTEGRINA.
SMARTSM00191. Int_alpha. 5 hits.
[Graphical view]
PROSITEPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP08514.
GeneWikiITGA2B.
GenomeRNAi3674.
NextBio14381.
PMAP-CutDBQ17R67.
PROP08514.
SOURCESearch...

Entry information

Entry nameITA2B_HUMAN
AccessionPrimary (citable) accession number: P08514
Secondary accession number(s): B2RCY8 expand/collapse secondary AC list , O95366, Q14443, Q17R67
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: April 14, 2009
Last modified: July 9, 2014
This is version 188 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries